ID TF2H2_RAT Reviewed; 396 AA. AC A0JN27; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 24-JAN-2024, entry version 117. DE RecName: Full=General transcription factor IIH subunit 2; DE AltName: Full=Basic transcription factor 2 44 kDa subunit; DE Short=BTF2 p44; DE AltName: Full=General transcription factor IIH polypeptide 2; DE AltName: Full=TFIIH basal transcription factor complex p44 subunit; GN Name=Gtf2h2; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-95, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=16641100; DOI=10.1073/pnas.0600895103; RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.; RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: RT regulation of aquaporin-2 phosphorylation at two sites."; RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006). CC -!- FUNCTION: Component of the general transcription and DNA repair factor CC IIH (TFIIH) core complex, which is involved in general and CC transcription-coupled nucleotide excision repair (NER) of damaged DNA CC and, when complexed to CAK, in RNA transcription by RNA polymerase II. CC In NER, TFIIH acts by opening DNA around the lesion to allow the CC excision of the damaged oligonucleotide and its replacement by a new CC DNA fragment. In transcription, TFIIH has an essential role in CC transcription initiation. When the pre-initiation complex (PIC) has CC been established, TFIIH is required for promoter opening and promoter CC escape. Phosphorylation of the C-terminal tail (CTD) of the largest CC subunit of RNA polymerase II by the kinase module CAK controls the CC initiation of transcription. The N-terminus of GTF2H2 interacts with CC and regulates XPD whereas an intact C-terminus is required for a CC successful escape of RNAP II form the promoter. CC {ECO:0000250|UniProtKB:Q13888}. CC -!- SUBUNIT: Component of the TFIID-containing RNA polymerase II pre- CC initiation complex that is composed of TBP and at least GTF2A1, GTF2A2, CC GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, CC ERCC2 and ERCC3. Component of the 7-subunit TFIIH core complex composed CC of XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and GTF2H5, CC which is active in NER. The core complex associates with the 3-subunit CC CDK-activating kinase (CAK) module composed of CCNH/cyclin H, CDK7 and CC MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in CC transcription. Interacts with XPB, XPD, GTF2H1 and GTF2H3. CC {ECO:0000250|UniProtKB:Q13888}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13888}. CC -!- SIMILARITY: Belongs to the GTF2H2 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC126097; AAI26098.1; -; mRNA. DR RefSeq; NP_001070896.1; NM_001077428.1. DR RefSeq; XP_006231906.1; XM_006231844.3. DR RefSeq; XP_006231907.1; XM_006231845.3. DR AlphaFoldDB; A0JN27; -. DR SMR; A0JN27; -. DR STRING; 10116.ENSRNOP00000057895; -. DR iPTMnet; A0JN27; -. DR PhosphoSitePlus; A0JN27; -. DR PaxDb; 10116-ENSRNOP00000057895; -. DR PeptideAtlas; A0JN27; -. DR Ensembl; ENSRNOT00000061183.4; ENSRNOP00000057895.2; ENSRNOG00000018230.8. DR Ensembl; ENSRNOT00055047004; ENSRNOP00055038624; ENSRNOG00055027191. DR Ensembl; ENSRNOT00060046094; ENSRNOP00060038283; ENSRNOG00060026612. DR Ensembl; ENSRNOT00065038375; ENSRNOP00065031085; ENSRNOG00065022496. DR GeneID; 294693; -. DR KEGG; rno:294693; -. DR UCSC; RGD:1310499; rat. DR AGR; RGD:1310499; -. DR CTD; 2966; -. DR RGD; 1310499; Gtf2h2. DR eggNOG; KOG2807; Eukaryota. DR GeneTree; ENSGT00490000043395; -. DR HOGENOM; CLU_028556_1_0_1; -. DR InParanoid; A0JN27; -. DR OrthoDB; 276422at2759; -. DR PhylomeDB; A0JN27; -. DR TreeFam; TF314037; -. DR Reactome; R-RNO-112382; Formation of RNA Pol II elongation complex. DR Reactome; R-RNO-113418; Formation of the Early Elongation Complex. DR Reactome; R-RNO-5696395; Formation of Incision Complex in GG-NER. DR Reactome; R-RNO-5696400; Dual Incision in GG-NER. DR Reactome; R-RNO-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-RNO-6781823; Formation of TC-NER Pre-Incision Complex. DR Reactome; R-RNO-6782135; Dual incision in TC-NER. DR Reactome; R-RNO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER. DR Reactome; R-RNO-6796648; TP53 Regulates Transcription of DNA Repair Genes. DR Reactome; R-RNO-72086; mRNA Capping. DR Reactome; R-RNO-73762; RNA Polymerase I Transcription Initiation. DR Reactome; R-RNO-73772; RNA Polymerase I Promoter Escape. DR Reactome; R-RNO-73776; RNA Polymerase II Promoter Escape. DR Reactome; R-RNO-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening. DR Reactome; R-RNO-73863; RNA Polymerase I Transcription Termination. DR Reactome; R-RNO-75953; RNA Polymerase II Transcription Initiation. DR Reactome; R-RNO-75955; RNA Polymerase II Transcription Elongation. DR Reactome; R-RNO-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance. DR Reactome; R-RNO-77075; RNA Pol II CTD phosphorylation and interaction with CE. DR PRO; PR:A0JN27; -. DR Proteomes; UP000002494; Chromosome 2. DR Bgee; ENSRNOG00000018230; Expressed in ovary and 19 other cell types or tissues. DR GO; GO:0000438; C:core TFIIH complex portion of holo TFIIH complex; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005669; C:transcription factor TFIID complex; ISO:RGD. DR GO; GO:0000439; C:transcription factor TFIIH core complex; ISO:RGD. DR GO; GO:0005675; C:transcription factor TFIIH holo complex; ISS:UniProtKB. DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:RGD. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0002031; P:G protein-coupled receptor internalization; ISO:RGD. DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; ISO:RGD. DR CDD; cd01453; vWA_transcription_factor_IIH_type; 1. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR046349; C1-like_sf. DR InterPro; IPR007198; Ssl1-like. DR InterPro; IPR004595; TFIIH_C1-like_dom. DR InterPro; IPR012170; TFIIH_SSL1/p44. DR InterPro; IPR002035; VWF_A. DR InterPro; IPR036465; vWFA_dom_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR NCBIfam; TIGR00622; ssl1; 1. DR PANTHER; PTHR12695; GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 2; 1. DR PANTHER; PTHR12695:SF2; GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 2-RELATED; 1. DR Pfam; PF07975; C1_4; 1. DR Pfam; PF04056; Ssl1; 1. DR PIRSF; PIRSF015919; TFIIH_SSL1; 1. DR SMART; SM01047; C1_4; 1. DR SMART; SM00327; VWA; 1. DR SUPFAM; SSF57889; Cysteine-rich domain; 1. DR SUPFAM; SSF53300; vWA-like; 1. DR PROSITE; PS50234; VWFA; 1. DR Genevisible; A0JN27; RN. PE 1: Evidence at protein level; KW DNA damage; DNA repair; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation; Zinc; KW Zinc-finger. FT CHAIN 1..396 FT /note="General transcription factor IIH subunit 2" FT /id="PRO_0000327566" FT DOMAIN 60..236 FT /note="VWFA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT ZN_FING 292..309 FT /note="C4-type" FT MOD_RES 95 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:16641100" SQ SEQUENCE 396 AA; 44703 MW; 2812ED7B0DC5B3C8 CRC64; MDEEPERTKR WEGGYERTWE ILKEDESGSL KATIEDILFK AKRKRVFEHH GQVRLGMMRH LYVVVDGSRT MEDQDLKPNR LTCTLKLLEY FVEEYFDQNP ISQIGIIVTK SKRAEKLTEL SGNPRKHITS LKKAVDMTCH GEPSLYNSLS MAMQTLKHMP GHTSREVLII FSSLTTCDPS NIYDLIKTLK TAKIRVSVIG LSAEVRVCTV LARETGGTYH VILDETHYKE LLARHVSPPP ASSGSECSLI RMGFPQHTIA SLSDQDAKPS FSMAHLDNNS TEPGLTLGGY FCPQCRAKYC ELPVECKICG LTLVSAPHLA RSYHHLFPLD AFQEIPLEEY KGERFCYGCQ GELKDQHVYV CTVCRNVFCV DCDVFVHDSL HCCPGCVHKI PTQSGV //